ID A0A0T5ZWR7_9BACT Unreviewed; 570 AA.
AC A0A0T5ZWR7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=protein-secreting ATPase {ECO:0000256|ARBA:ARBA00024382};
DE EC=7.4.2.8 {ECO:0000256|ARBA:ARBA00024382};
GN ORFNames=XU13_C0103G0006 {ECO:0000313|EMBL:KRT67211.1};
OS Candidatus Rokubacteria bacterium CSP1-6.
OC Bacteria; Candidatus Rokubacteria.
OX NCBI_TaxID=1640509 {ECO:0000313|EMBL:KRT67211.1, ECO:0000313|Proteomes:UP000051916};
RN [1] {ECO:0000313|EMBL:KRT67211.1, ECO:0000313|Proteomes:UP000051916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-6 {ECO:0000313|EMBL:KRT67211.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00034006};
CC -!- SIMILARITY: Belongs to the GSP E family.
CC {ECO:0000256|ARBA:ARBA00006611}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT67211.1}.
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DR EMBL; LDXP01000103; KRT67211.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZWR7; -.
DR STRING; 1640509.XU13_C0103G0006; -.
DR PATRIC; fig|1640509.3.peg.2791; -.
DR Proteomes; UP000051916; Unassembled WGS sequence.
DR GO; GO:0015627; C:type II protein secretion system complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IEA:InterPro.
DR CDD; cd01129; PulE-GspE-like; 1.
DR Gene3D; 3.30.450.90; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.300.160; Type II secretion system, protein E, N-terminal domain; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS_dom.
DR InterPro; IPR037257; T2SS_E_N_sf.
DR InterPro; IPR013369; T2SS_GspE.
DR InterPro; IPR007831; T2SS_GspE_N.
DR NCBIfam; TIGR02533; type_II_gspE; 1.
DR PANTHER; PTHR30258:SF2; BACTERIOPHAGE ADSORPTION PROTEIN B; 1.
DR PANTHER; PTHR30258; TYPE II SECRETION SYSTEM PROTEIN GSPE-RELATED; 1.
DR Pfam; PF05157; MshEN; 1.
DR Pfam; PF00437; T2SSE; 1.
DR SUPFAM; SSF160246; EspE N-terminal domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00662; T2SP_E; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 385..399
FT /note="Bacterial type II secretion system protein E"
FT /evidence="ECO:0000259|PROSITE:PS00662"
SQ SEQUENCE 570 AA; 62564 MW; 77F6800B4632CB3E CRC64;
MAISVAKLPL GQLLLDAGLI TPDILREALA RQKTTRAPIG EVLVAMGAVG KDDVLRAVAQ
QQGLPYLTRD ELPSSVPVLK NLSPKYLRQY RVCPVAMEGS ALTVATSDPV NPLLQDDLRQ
ALGLQIKLAV APEDAILETI ERTYGAGAAS PLQRIVEGIR EEGLAPGEGE EDINQLRDMA
FEAPVVRLVN LLIENAVTAE ASDIHIEPFE DTLRVRYRID GLLFDQEAPP RRLQAAVTSR
IKIMAELNIA ERRLPQDGRI RVTLGGRRVD IRVSTIPTLY GESIVMRLLD RSSIFLPLEK
LGFSPDTRRL FERLIVRPHG MLLVTGPTGS GKTTTLYGAL DKINSPEKKI ITIEDPVEYQ
LKGVNQIAVK PKIGLSFANG LRHIVRQDPD IIMVGEVRDL ETGEIAIQAA LTGHLVFSTL
HTNDAPGAIT RLQDMGCEPY LVSSVLHGVL AQRLVRRICL ACRAPHTADL ADLRALGIPE
ALDEPQNLYK GAGCDQCRGT GYRGRTGIYE LFVINEDVRS LIVRKAPTGE IRRQATHELG
MVTLREDGWA KAKLGVTTID EVLRVTQEEE
//